ID A0A091N0K8_9PASS Unreviewed; 356 AA.
AC A0A091N0K8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Decorin {ECO:0000256|ARBA:ARBA00021503, ECO:0000256|RuleBase:RU364097};
DE AltName: Full=Bone proteoglycan II {ECO:0000256|RuleBase:RU364097};
DE Flags: Fragment;
GN ORFNames=N310_12987 {ECO:0000313|EMBL:KFP82472.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP82472.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP82472.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP82472.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May affect the rate of fibrils formation.
CC {ECO:0000256|RuleBase:RU364097}.
CC -!- SUBUNIT: Binds to type I and type II collagen, fibronectin and TGF-
CC beta. Forms a ternary complex with MFAP2 and ELN.
CC {ECO:0000256|RuleBase:RU364097}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU364097}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class I subfamily. {ECO:0000256|ARBA:ARBA00009811,
CC ECO:0000256|RuleBase:RU364097}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK839722; KFP82472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091N0K8; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR016352; SLRP_I_decor/aspor/byglycan.
DR PANTHER; PTHR45712; AGAP008170-PA; 1.
DR PANTHER; PTHR45712:SF14; DECORIN; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01462; LRRNT; 1.
DR PIRSF; PIRSF002490; SLRP_I; 1.
DR SMART; SM00364; LRR_BAC; 4.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002490-1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530,
KW ECO:0000256|RuleBase:RU364097};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022974};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364097};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..356
FT /note="Decorin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013085102"
FT DOMAIN 50..82
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
FT DISULFID 51..57
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 55..64
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 310..343
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP82472.1"
FT NON_TER 356
FT /evidence="ECO:0000313|EMBL:KFP82472.1"
SQ SEQUENCE 356 AA; 39475 MW; 574D6F989875C97D CRC64;
RLALLFTLLL PACLAKPFHQ QGLFDFMLED EGSADMPSTD DPVISGFGPV CPFRCQCHLR
VVQCSDLGLE KVPKDLPPDT TLLDLQNNKI TEIREGDFKN VKNLHALILV NNKISKISPL
AFAPLKKLER LYLSKNSLKE LPENMPKSLQ EIRAHENEIS KLRKAVFNGL NQVIVLELGT
NPIKSSGIEN GAFQGMKRLS YIRIADTNIT TIPKGLPPSL TELHLDGNKI SKIDAESLSG
LTNLAKLGLS FNSISSVENG SLNNVPHLRE LHLNNNALNR VPSGLGEHKY IQVVYLHNNN
ISSIGINDFC PLGYNTKKAS YSGVSLFSNP VQYWEIQPSA FRCIHERSAV QIGNYK
//
